The development of a set of transferable intermolecular potential functions (TIPS) describing water-protein interactions is proposed. This represents an extension of the TIPS for water, alkanes, alcohols, and ethers that have already been demonstrated to yield good thermodynamic and structural results for pure liquids and dilute solutions in statistical mechanics simulations. The TIPS parameters for biochemical systems will be chosen to reproduce experimental data for pure liquid amides, for aqueous solutions of amides and for various organic systems representing side chains. Comparisons will also be made with high quality ab initio quantum mechanical calculations for hydrogen bonded complexes. The proposed work will entail numerous Monte Carlo simulations of pure liquids and aqueous solutions that will yield detailed insights into the hydration of protein constituents, the nature of hydrophobic effects and the structure of liquid amides. The availability of TIPS for biochemical systems will be of great utility to biophysicists interested in studying problems such as the hydration of macromolecules including the location of localized water molecules in protein crystals and in active sites of enzymes, enzyme-substrate binding, the conformations of polypeptides and their denaturation.